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PIP kinase Igamma is the major PI(4,5)P(2) synthesizing enzyme at the synapse.

Authors: Wenk, M R  Pellegrini, L  Klenchin, V A  Di Paolo, G  Chang, S  Daniell, L  Arioka, M  Martin, T F  De Camilli, P 
Citation: Wenk MR, etal., Neuron. 2001 Oct 11;32(1):79-88.
Pubmed: (View Article at PubMed) PMID:11604140

Disruption of the presynaptically enriched polyphosphoinositide phosphatase synaptojanin 1 leads to an increase of clathrin-coated intermediates and of polymerized actin at endocytic zones of nerve terminals. These changes correlate with elevated levels of PI(4,5)P(2) in neurons. We report that phosphatidylinositol phosphate kinase type Igamma (PIPKIgamma), a major brain PI(4)P 5-kinase, is concentrated at synapses. Synaptojanin 1 and PIPKIgamma antagonize each other in the recruitment of clathrin coats to lipid membranes. Like synaptojanin 1 and other proteins involved in endocytosis, PIPKIgamma undergoes stimulation-dependent dephosphorylation. These results implicate PIPKIgamma in the synthesis of a PI(4,5)P(2) pool that acts as a positive regulator of clathrin coat recruitment and actin function at the synapse.


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CRRD Object Information
CRRD ID: 13702138
Created: 2018-07-18
Species: All species
Last Modified: 2018-07-18
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.